SYA2_LACP7
ID SYA2_LACP7 Reviewed; 591 AA.
AC A9KLZ5;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Alanine--tRNA ligase 2;
DE EC=6.1.1.7;
DE AltName: Full=Alanyl-tRNA synthetase 2;
DE Short=AlaRS 2;
GN Name=alaS2; OrderedLocusNames=Cphy_0956;
OS Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg)
OS (Clostridium phytofermentans).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=357809;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700394 / DSM 18823 / ISDg;
RA Leschine S.B., Warnick T.A., Blanchard J.L., Schnell D.J., Petit E.L.,
RA LaTouf W.G., Copeland A., Lucas S., Lapidus A., Barry K.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA Bruce D., Detter J.C., Han C., Kuske C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E.A., Richardson P.;
RT "Complete genome sequence of Clostridium phytofermentans ISDg.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a two-
CC step reaction: alanine is first activated by ATP to form Ala-AMP and
CC then transferred to the acceptor end of tRNA(Ala). Also edits
CC incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing
CC domain (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-
CC tRNA(Ala); Xref=Rhea:RHEA:12540, Rhea:RHEA-COMP:9657, Rhea:RHEA-
CC COMP:9923, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78497, ChEBI:CHEBI:456215; EC=6.1.1.7;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: Consists of three domains; the N-terminal catalytic domain, the
CC editing domain and the C-terminal C-Ala domain. The editing domain
CC removes incorrectly charged amino acids, while the C-Ala domain, along
CC with tRNA(Ala), serves as a bridge to cooperatively bring together the
CC editing and aminoacylation centers thus stimulating deacylation of
CC misacylated tRNAs (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; CP000885; ABX41338.1; -; Genomic_DNA.
DR RefSeq; WP_012198983.1; NC_010001.1.
DR AlphaFoldDB; A9KLZ5; -.
DR SMR; A9KLZ5; -.
DR STRING; 357809.Cphy_0956; -.
DR EnsemblBacteria; ABX41338; ABX41338; Cphy_0956.
DR KEGG; cpy:Cphy_0956; -.
DR eggNOG; COG0013; Bacteria.
DR HOGENOM; CLU_004485_0_2_9; -.
DR OMA; WVEVWNH; -.
DR OrthoDB; 91428at2; -.
DR Proteomes; UP000000370; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00036_B; Ala_tRNA_synth_B; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR002318; Ala-tRNA-lgiase_IIc.
DR InterPro; IPR018162; Ala-tRNA-ligase_IIc_anticod-bd.
DR InterPro; IPR018165; Ala-tRNA-synth_IIc_core.
DR InterPro; IPR018164; Ala-tRNA-synth_IIc_N.
DR InterPro; IPR023033; Ala_tRNA_ligase_euk/bac.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR012947; tRNA_SAD.
DR Pfam; PF01411; tRNA-synt_2c; 1.
DR Pfam; PF07973; tRNA_SAD; 1.
DR PRINTS; PR00980; TRNASYNTHALA.
DR SMART; SM00863; tRNA_SAD; 1.
DR SUPFAM; SSF101353; SSF101353; 1.
DR SUPFAM; SSF55186; SSF55186; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding;
KW tRNA-binding; Zinc.
FT CHAIN 1..591
FT /note="Alanine--tRNA ligase 2"
FT /id="PRO_0000347572"
FT BINDING 453
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 457
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 555
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 559
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
SQ SEQUENCE 591 AA; 67558 MW; 8668C8B00DD6A5DB CRC64;
MTANELRKMY VDYFKERGHQ EIASASLLPE NDPTVLFTTA GMHPLVPYLL GENHPKGTRL
VSVQKCVRTG DIDEVGDDTH LTFFEMLGNW SLGEYFKEES ISISYDFLTT CLNIPKEKLA
VTVFEGDELV PRDEEVSQTW KSKGLQDNQI FYYGREENWW GPAGQTGPCG TDTEIFYDMG
KPSCGVNCGP ACDCGKYVEI WNNVFMQYHK KPDGSYEEMK QKNVDTGMGF ERVLTILNGY
TNVYETELFL PVKNRLDEII EANEAKLSEK SKRIICEHIR AVTFLLGDPK MIVPSNSEQG
YILRRLIRRM IRHLKQVSIE NNVLCKLSKV IVEQYGSIYV ELRENELFIM EQLEKEYDLF
SKTLDRGLKN AKLYFDQVGE EKILNGELSF KLYDTFGFPI EFTIELASEM EITVDVEAYN
QKFAEHQKKS RQGAEVKFKG GLSDHGEQTT RLHTATHLLN GALRTVLGTD VFQRGSNITE
ERLRFDFSFH RKLTKEELEE VERIVNEAIR NQIDVLCEEM TVKEAKELGA VGIFEDKYGE
VVKVYMIPGY SKEICGGPHV KNTSELKSFR TVKEEASSAG VRRIKAVIGS N
